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Article

Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms.

PloS one - 1 Jan 2012

Thomas Elaine C, Gunter Jennifer H, Webster Julie A, Schieber Nicole L, Oorschot Viola, Parton Robert G, Whitehead Jonathan P

Abstract excerpt

We recently reported that Inosine Monophosphate Dehydrogenase (IMPDH), a rate-limiting enzyme in de novo guanine nucleotide biosynthesis, clustered into macrostructures in response to decreased nucleotide levels and that there were differences between the IMPDH isoforms, IMPDH1 and IMPDH2. We hypothesised that the Bateman domains, which are present in both isoforms and serve as energy-sensing/allosteric modules...

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Identifiers

PMID: 23236438
DOI: 10.1371/journal.pone.0051096
PMCID: PMC3517587

Genes

IMPDH1
IMPDH2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms.PMID 23236438Read ↗

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